OSPF_SHIFL
ID OSPF_SHIFL Reviewed; 239 AA.
AC Q8VSP9; Q2ET10; Q2ET14; Q6XW10; Q7BEG0; Q99Q87;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Phosphothreonine lyase OspF;
DE EC=4.2.3.-;
DE AltName: Full=Effector protein OspF;
GN Name=ospF; Synonyms=mkaD; OrderedLocusNames=CP0010;
GN ORFNames=pWR501_0013, SFLP011;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pCP301, Plasmid pSF5, Plasmid pINV_F6_M1382,
OG Plasmid pSf2b_251, Plasmid pSf1a_571, Plasmid pSfx_580, Plasmid pSf6_579,
OG Plasmid pSf3_575, Plasmid pSf4a_576, Plasmid pSf4b_577, and
OG Plasmid pSf5_246.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M1382 / Serotype 6; PLASMID=pINV_F6_M1382;
RX PubMed=14573649; DOI=10.1128/iai.71.11.6298-6306.2003;
RA Lan R., Stevenson G., Reeves P.R.;
RT "Comparison of two major forms of the Shigella virulence plasmid pINV:
RT positive selection is a major force driving the divergence.";
RL Infect. Immun. 71:6298-6306(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype 5; PLASMID=pSF5;
RX PubMed=16704117; DOI=10.1007/s11427-006-0141-3;
RA Xiong Z., Tang X., Yang F., Zhang X., Yang J., Chen L., Nie H., Yan Y.,
RA Jiang Y., Wang J., Xue Y., Xu X., Zhu Y., Dong J., An L., Wang X., Jin Q.;
RT "Comparison of the virulence plasmid genomes of two strains of Shigella
RT which lost the ability to bind Congo red.";
RL Sci. China, Ser. C, Life Sci. 49:141-148(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-192.
RC STRAIN=246 / Serotype 5, 251 / Serotype 2b, 571 / Serotype 1a,
RC 575 / Serotype 3, 576 / Serotype 4a, 577 / Serotype 4b, 579 / Serotype 6,
RC and 580;
RC PLASMID=pSf1a_571, pSf2b_251, pSf3_575, pSf4a_576, pSf4b_577, pSf5_246,
RC pSf6_579, and pSfx_580;
RX PubMed=17160643; DOI=10.1007/s00239-006-0052-8;
RA Yang J., Nie H., Chen L., Zhang X., Yang F., Xu X., Zhu Y., Yu J., Jin Q.;
RT "Revisiting the molecular evolutionary history of Shigella spp.";
RL J. Mol. Evol. 64:71-79(2007).
RN [7]
RP REGULATION BY MXIE, AND INDUCTION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=12142411; DOI=10.1128/jb.184.16.4409-4419.2002;
RA Kane C.D., Schuch R., Day W.A. Jr., Maurelli A.T.;
RT "MxiE regulates intracellular expression of factors secreted by the
RT Shigella flexneri 2a type III secretion system.";
RL J. Bacteriol. 184:4409-4419(2002).
RN [8]
RP REGULATION BY MXIE AND IPGC.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=12446624; DOI=10.1128/jb.184.24.6751-6759.2002;
RA Mavris M., Sansonetti P.J., Parsot C.;
RT "Identification of the cis-acting site involved in activation of promoters
RT regulated by activity of the type III secretion apparatus in Shigella
RT flexneri.";
RL J. Bacteriol. 184:6751-6759(2002).
RN [9]
RP REGULATION BY MXIE AND VIRB.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=15758240; DOI=10.1099/mic.0.27639-0;
RA Le Gall T., Mavris M., Martino M.C., Bernardini M.L., Denamur E.,
RA Parsot C.;
RT "Analysis of virulence plasmid gene expression defines three classes of
RT effectors in the type III secretion system of Shigella flexneri.";
RL Microbiology 151:951-962(2005).
RN [10]
RP ACTIVATION OF MEK/ERK, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=16988276; DOI=10.1128/iai.00594-06;
RA Zurawski D.V., Mitsuhata C., Mumy K.L., McCormick B.A., Maurelli A.T.;
RT "OspF and OspC1 are Shigella flexneri type III secretion system effectors
RT that are required for postinvasion aspects of virulence.";
RL Infect. Immun. 74:5964-5976(2006).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=17159983; DOI=10.1038/ni1423;
RA Arbibe L., Kim D.W., Batsche E., Pedron T., Mateescu B., Muchardt C.,
RA Parsot C., Sansonetti P.J.;
RT "An injected bacterial effector targets chromatin access for transcription
RT factor NF-kappaB to alter transcription of host genes involved in immune
RT responses.";
RL Nat. Immunol. 8:47-56(2007).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=17305427; DOI=10.1371/journal.ppat.0030021;
RA Kramer R.W., Slagowski N.L., Eze N.A., Giddings K.S., Morrison M.F.,
RA Siggers K.A., Starnbach M.N., Lesser C.F.;
RT "Yeast functional genomic screens lead to identification of a role for a
RT bacterial effector in innate immunity regulation.";
RL PLoS Pathog. 3:179-190(2007).
RN [13]
RP FUNCTION, PHOSPHOTHREONINE LYASE ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP AND MUTAGENESIS OF ASP-101; LYS-102; HIS-104; ASP-127; ASP-131; LYS-134;
RP ASP-137; ASP-160; ARG-175 AND ARG-218.
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=17303758; DOI=10.1126/science.1138960;
RA Li H., Xu H., Zhou Y., Zhang J., Long C., Li S., Chen S., Zhou J.-M.,
RA Shao F.;
RT "The phosphothreonine lyase activity of a bacterial type III effector
RT family.";
RL Science 315:1000-1003(2007).
CC -!- FUNCTION: Catalyzes the removal of the phosphate group from the
CC phosphothreonine in the mitogen-activated protein kinases such as
CC MAPK2/ERK2, MAPK3/ERK1, MAPK8 and MAPK14 in an irreversible reaction,
CC thus preventing the downstream phosphorylation of histone H3. This
CC epigenetic modification results in inhibition of the transcription of a
CC specific subset of pro-inflammatory genes, and ultimately to a reduced
CC immune response against the invading pathogen. The diminished immune
CC response enhances the bacterium's ability to disseminate and multiply
CC within the host. {ECO:0000269|PubMed:17159983,
CC ECO:0000269|PubMed:17303758, ECO:0000269|PubMed:17305427}.
CC -!- ACTIVITY REGULATION: Inhibited by the tyrosine phosphatase inhibitor
CC vanadate. {ECO:0000269|PubMed:17159983}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=204 nM for phosphorylated MAPK2 (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17159983, ECO:0000269|PubMed:17303758};
CC Vmax=9.89 pM/sec/ug enzyme with phosphorylated MAPK2 as substrate (at
CC pH 8 and 30 degrees Celsius) {ECO:0000269|PubMed:17159983,
CC ECO:0000269|PubMed:17303758};
CC -!- INTERACTION:
CC Q8VSP9; P28482: MAPK1; Xeno; NbExp=5; IntAct=EBI-6506625, EBI-959949;
CC Q8VSP9; P06400: RB1; Xeno; NbExp=2; IntAct=EBI-6506625, EBI-491274;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11115111,
CC ECO:0000269|PubMed:16988276, ECO:0000269|PubMed:17159983,
CC ECO:0000269|PubMed:17305427}. Note=Secreted via the type III secretion
CC system (TTSS). Localizes in the nucleus of the infected cell.
CC -!- INDUCTION: Transcriptionally activated by MxiE in the intracellular
CC environment of the host, in association with IpgC, under conditions of
CC deregulated or active secretion. Expressed in a VirB-dependent but
CC MxiE-independent way under conditions of non-secretion.
CC {ECO:0000269|PubMed:12142411}.
CC -!- SIMILARITY: Belongs to the phosphothreonine lyase family.
CC {ECO:0000305}.
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DR EMBL; AL391753; CAC05773.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18324.1; -; Genomic_DNA.
DR EMBL; AY206429; AAP78969.1; -; Genomic_DNA.
DR EMBL; AY879342; AAW64770.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72315.1; -; Genomic_DNA.
DR EMBL; DQ362850; ABD37257.1; -; Genomic_DNA.
DR EMBL; DQ362864; ABD37271.1; -; Genomic_DNA.
DR EMBL; DQ362865; ABD37272.1; -; Genomic_DNA.
DR EMBL; DQ362866; ABD37273.1; -; Genomic_DNA.
DR EMBL; DQ362867; ABD37274.1; -; Genomic_DNA.
DR EMBL; DQ362868; ABD37275.1; -; Genomic_DNA.
DR EMBL; DQ362869; ABD37276.1; -; Genomic_DNA.
DR EMBL; DQ362870; ABD37277.1; -; Genomic_DNA.
DR RefSeq; NP_858143.1; NC_004851.1.
DR RefSeq; WP_001121867.1; NZ_WPGT01000181.1.
DR RefSeq; WP_010921598.1; NZ_QWST01000360.1.
DR RefSeq; YP_006960239.1; NC_019197.1.
DR PDB; 3I0U; X-ray; 2.70 A; A/B=23-239.
DR PDBsum; 3I0U; -.
DR AlphaFoldDB; Q8VSP9; -.
DR SMR; Q8VSP9; -.
DR IntAct; Q8VSP9; 3.
DR MINT; Q8VSP9; -.
DR STRING; 198214.CP0010; -.
DR EnsemblBacteria; AAL72315; AAL72315; SF_p0010.
DR GeneID; 1238011; -.
DR KEGG; sfl:CP0010; -.
DR HOGENOM; CLU_100525_0_0_6; -.
DR OMA; RVDQQSR; -.
DR SABIO-RK; Q8VSP9; -.
DR EvolutionaryTrace; Q8VSP9; -.
DR PRO; PR:Q8VSP9; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2430.10; -; 1.
DR InterPro; IPR003519; OspF/SpvC.
DR InterPro; IPR038498; OspF/SpvC_sf.
DR Pfam; PF03536; VRP3; 1.
DR PRINTS; PR01342; SALVRPPROT.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase; Plasmid;
KW Reference proteome; Secreted; Virulence.
FT CHAIN 1..239
FT /note="Phosphothreonine lyase OspF"
FT /id="PRO_0000299354"
FT ACT_SITE 104
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT VARIANT 19
FT /note="R -> K (in plasmid pWR100 and plasmid pSF5)"
FT VARIANT 66
FT /note="S -> F (in plasmid pWR100, plasmid pSF5, plasmid
FT pINV_F6_M1382, plasmid pSf6_579, plasmid pSf3_575, plasmid
FT pSf4a_576, plasmid pSf4b_577 and plasmid pSf5_246)"
FT MUTAGEN 101
FT /note="D->A: No change in Erk2 phosphothreonine lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 102
FT /note="K->R: Loss of Erk2 phosphothreonine lyase activity.
FT No effect in binding ability to erk. Deficient in down-
FT regulating MAPK signaling."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 104
FT /note="H->A: Loss of Erk2 phosphothreonine lyase activity.
FT No effect in binding ability to erk. Deficient in down-
FT regulating MAPK signaling."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 127
FT /note="D->A: No change in Erk2 phosphothreonine lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 131
FT /note="D->A: No change in Erk2 phosphothreonine lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 134
FT /note="K->A: Loss of Erk2 phosphothreonine lyase activity.
FT No effect in binding ability to erk. Deficient in down-
FT regulating MAPK signaling."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 137
FT /note="D->A: No change in Erk2 phosphothreonine lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 160
FT /note="D->A: No change in Erk2 phosphothreonine lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 175
FT /note="R->A: No change in Erk2 phosphothreonine lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:17303758"
FT MUTAGEN 218
FT /note="R->A: No change in Erk2 phosphothreonine lyase
FT activity."
FT /evidence="ECO:0000269|PubMed:17303758"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:3I0U"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:3I0U"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3I0U"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:3I0U"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:3I0U"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:3I0U"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:3I0U"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:3I0U"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:3I0U"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3I0U"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:3I0U"
FT HELIX 168..187
FT /evidence="ECO:0007829|PDB:3I0U"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:3I0U"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:3I0U"
SQ SEQUENCE 239 AA; 27828 MW; 75F6EA2D6FFD002A CRC64;
MPIKKPCLKL NLDSLNVVRS EIPQMLSANE RLKNNFNILY NQIRQYPAYY FKVASNVPTY
SDICQSFSVM YQGFQIVNHS GDVFIHACRE NPQSKGDFVG DKFHISIARE QVPLAFQILS
GLLFSEDSPI DKWKITDMNR VSQQSRVGIG AQFTLYVKSD QECSQYSALL LHKIRQFIMC
LESNLLRSKI APGEYPASDV RPEDWKYVSY RNELRSDRDG SERQEQMLRE EPFYRLMIE
